2.4.1.258: dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase
This is an abbreviated version!
For detailed information about dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.258
-
2.4.1.258
-
n-glycosylation
-
n-glycans
-
lipid-linked
-
oligosaccharide
-
glc3man9glcnac2
-
glycan
-
medicine
-
peptide-n-glycosidase
-
synthesis
- 2.4.1.258
-
n-glycosylation
- n-glycans
-
lipid-linked
- oligosaccharide
- glc3man9glcnac2
- glycan
- medicine
-
peptide-n-glycosidase
- synthesis
Reaction
Synonyms
Alg3, Alg3p, AtALG3, Dol-P-Man:Man5GlcNAc2-PP-Dol alpha1,3-mannosyl transferase, Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase, dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase, EC 2.4.1.130, Not56-like protein, PpAlg3 alpha-1,3-mannosyl transferase, TbALG3
ECTree
Advanced search results
Application
Application on EC 2.4.1.258 - dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
medicine
synthesis
-
genetic engineering of N-glycan biosynthesis in Yarrowia lipolytica so that it produces Man(3)GlcNAc(2) structures on its glycoproteins. Disruption of the ALG3 gene, EC 2.4.1.258, results in modification of proteins mainly with Man(5)GlcNAc(2) and GlcMan(5)GlcNAc(2) glycans, and to a lesser extent with Glc(2)Man(5)GlcNAc(2) glycans. To avoid underoccupancy of glycosylation sites, Alg6, EC 2.4.1.267, is concomitantly overexpressed. Overexpression of the heterodimeric Aspergillus niger glucosidase II results in removal the terminal glucose residues. Overexpression of an alpha-1,2-mannosidase leads to Man(3)GlcNAc(2) structures, which are substrates for the synthesis of complex-type glycans. The final Yarrowia lipolytica strain produces proteins glycosylated with the trimannosyl core N-glycan (Man(3)GlcNAc(2)), which is the common core of all complex-type N-glycans
-
two Vietnamese siblings with confirmed ALG3-Congenital disorders of glycosylation, 15 and 21 years old, show clinical features with previously reported patients including facial dysmorphism, severe psychomotor retardation, microcephaly, seizures, and gastrointestinal symptoms. Both patients show mutations c.206T > C (p.169 T) and c.626T > C (p.M209T)
medicine
identification of an additional open-reading frame of 141 bp (AAGRP) in the coding region of ALG3 in a patient with congenital disorder of glycosylation. Expression of this hybrid protein is significantly increased due to the homozygous variant c.160_196del. Patient shows secondary microcephaly, significantly decreased head control and axial muscular hypotonia associated with increased limb stiffness. Frequent episodes of hyperextension are observed